4hyb - Revision history

OCA at 08:26, 9 November 2022

2022-11-09T08:26:02Z

←Older revision		Revision as of 08:26, 9 November 2022
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	==Crystal structure of the substrate binding domain of E.coli DnaK in complex with pyrrhocoricin_LYZI (residues 1 to 10)==		==Crystal structure of the substrate binding domain of E.coli DnaK in complex with pyrrhocoricin_LYZI (residues 1 to 10)==
-	<StructureSection load='4hyb' size='340' side='right' caption='[[4hyb]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='4hyb' size='340' side='right'caption='[[4hyb]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4hyb]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HYB OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4HYB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4hyb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Pyrrhocoris_apterus Pyrrhocoris apterus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HYB FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALC:2-AMINO-3-CYCLOHEXYL-PROPIONIC+ACID'>ALC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr~~ id~~='NonStdRes'><td class~~="~~sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat~~"><scene name='pdbligand=ALC:2-AMINO-3-CYCLOHEXYL-PROPIONIC+ACID'>ALC</scene><~~/td></tr>~~	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4hyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hyb OCA], [https://pdbe.org/4hyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hyb RCSB], [https://www.ebi.ac.uk/pdbsum/4hyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hyb ProSAT]</span></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b></td><td class="sblockDat">[[1dkx\|1dkx]], [[1dky\|1dky]], [[1dkz\|1dkz]], [[3dpo\|3dpo]], [[3dpp\|3dpp]], [[3dpq\|3dpq]], [[3qnj\|3qnj]], [[4e81\|4e81]], [[4hy9\|4hy9]]</td></tr>~~	+
-	~~<tr id='gene~~'>~~<td class="sblockLbl"><b>[[Gene\|Gene:]]~~</b>~~</td><td class="sblockDat">dnaK, groP, grpF, seg, b0014, JW0013 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])~~</td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4hyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hyb OCA], [~~http~~://pdbe.org/4hyb PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4hyb RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4hyb PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4hyb ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DNAK_ECOLI DNAK_ECOLI]] Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.[HAMAP-Rule:MF_00332] [[http://www.uniprot.org/uniprot/PYRRH_PYRAP PYRRH_PYRAP]] Antibacterial peptide. Affects Gram-negative bacteria E.coli 1106, P.aeruginosa, E.coli D22 and E.cloacae and Gram-positive bacteria M.luteus and B.subtilis.	+	[https://www.uniprot.org/uniprot/DNAK_ECOLI DNAK_ECOLI] Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.[HAMAP-Rule:MF_00332]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 4hyb" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4hyb" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Heat Shock Protein structures\|Heat Shock Protein structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ecoli~~]]	+	[[Category: Escherichia coli K-12]]
-	[[Category: ~~Straeter, N~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Zahn, M~~]]	+	[[Category: Pyrrhocoris apterus]]
-	[[Category: ~~Antimicrobial peptide~~]]	+	[[Category: Straeter N]]
-	[[Category: ~~Chaperone]]~~	+	[[Category: Zahn M]]
-	~~[[Category: Peptide binding protein~~]]	+

OCA at 08:47, 15 November 2017

2017-11-15T08:47:11Z

←Older revision		Revision as of 08:47, 15 November 2017
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	</div>		</div>
	<div class="pdbe-citations 4hyb" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4hyb" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Heat Shock Proteins\|Heat Shock Proteins]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:45, 4 August 2016

2016-08-04T13:45:26Z

←Older revision		Revision as of 13:45, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the substrate binding domain of E.coli DnaK in complex with pyrrhocoricin_LYZI (residues 1 to 10)==		==Crystal structure of the substrate binding domain of E.coli DnaK in complex with pyrrhocoricin_LYZI (residues 1 to 10)==
	<StructureSection load='4hyb' size='340' side='right' caption='[[4hyb]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='4hyb' size='340' side='right' caption='[[4hyb]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4hyb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli_k-12 Escherichia coli k-12~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HYB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HYB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4hyb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HYB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HYB FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALC:2-AMINO-3-CYCLOHEXYL-PROPIONIC+ACID'>ALC</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALC:2-AMINO-3-CYCLOHEXYL-PROPIONIC+ACID'>ALC</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dkx\|1dkx]], [[1dky\|1dky]], [[1dkz\|1dkz]], [[3dpo\|3dpo]], [[3dpp\|3dpp]], [[3dpq\|3dpq]], [[3qnj\|3qnj]], [[4e81\|4e81]], [[4hy9\|4hy9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dkx\|1dkx]], [[1dky\|1dky]], [[1dkz\|1dkz]], [[3dpo\|3dpo]], [[3dpp\|3dpp]], [[3dpq\|3dpq]], [[3qnj\|3qnj]], [[4e81\|4e81]], [[4hy9\|4hy9]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dnaK, groP, grpF, seg, b0014, JW0013 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ~~Escherichia coli K-12~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dnaK, groP, grpF, seg, b0014, JW0013 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hyb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hyb RCSB], [http://www.ebi.ac.uk/pdbsum/4hyb PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hyb OCA], [http://pdbe.org/4hyb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hyb RCSB], [http://www.ebi.ac.uk/pdbsum/4hyb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hyb ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4hyb" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Heat Shock Proteins\|Heat Shock Proteins]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia coli k-12~~]]	+	[[Category: Ecoli]]
	[[Category: Straeter, N]]		[[Category: Straeter, N]]
	[[Category: Zahn, M]]		[[Category: Zahn, M]]

OCA at 09:51, 25 December 2014

2014-12-25T09:51:13Z

←Older revision		Revision as of 09:51, 25 December 2014
Line 9:		Line 9:
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hyb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hyb RCSB], [http://www.ebi.ac.uk/pdbsum/4hyb PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hyb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hyb RCSB], [http://www.ebi.ac.uk/pdbsum/4hyb PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DNAK_ECOLI DNAK_ECOLI]] Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.[HAMAP-Rule:MF_00332] [[http://www.uniprot.org/uniprot/PYRRH_PYRAP PYRRH_PYRAP]] Antibacterial peptide. Affects Gram-negative bacteria E.coli 1106, P.aeruginosa, E.coli D22 and E.cloacae and Gram-positive bacteria M.luteus and B.subtilis.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 12:31, 21 December 2014

2014-12-21T12:31:40Z

←Older revision		Revision as of 12:31, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4hyb\| PDB=4hyb \| SCENE= }}~~	+	==Crystal structure of the substrate binding domain of E.coli DnaK in complex with pyrrhocoricin_LYZI (residues 1 to 10)==
-	===Crystal structure of the substrate binding domain of E.coli DnaK in complex with pyrrhocoricin_LYZI (residues 1 to 10)===	+	<StructureSection load='4hyb' size='340' side='right' caption='[[4hyb]], [[Resolution\|resolution]] 1.70Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23562829}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4hyb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HYB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HYB FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALC:2-AMINO-3-CYCLOHEXYL-PROPIONIC+ACID'>ALC</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dkx\|1dkx]], [[1dky\|1dky]], [[1dkz\|1dkz]], [[3dpo\|3dpo]], [[3dpp\|3dpp]], [[3dpq\|3dpq]], [[3qnj\|3qnj]], [[4e81\|4e81]], [[4hy9\|4hy9]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dnaK, groP, grpF, seg, b0014, JW0013 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hyb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hyb RCSB], [http://www.ebi.ac.uk/pdbsum/4hyb PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Hsp70 chaperones have been implicated in assisting protein folding of newly synthesized polypeptide chains, refolding of misfolded proteins, and protein trafficking. For these functions, the chaperones need to exhibit a significant promiscuity in binding to different sequences of hydrophobic peptide stretches. To characterize the structural basis of sequence specificity and flexibility of the Escherichia coli Hsp70 chaperone DnaK, we have analyzed crystal structures of the substrate binding domain of the protein in complex with artificially designed peptides as well as small proline-rich antimicrobial peptides. Proline-rich antimicrobial peptides from mammals and insects were identified to target DnaK after cell penetration. Interestingly, the complex crystal structures reveal two different peptide binding modes. The peptides can bind either in a forward or in a reverse direction to the conventional substrate binding cleft of DnaK in an extended conformation. Superposition of the two binding modes shows a remarkable similarity in the side-chain orientations and hydrogen-bonding pattern despite the reversed peptide orientation. The DnaK chaperone has evolved to bind peptides in both orientations in the substrate binding cleft with comparable energy without rearrangements of the protein. Optimal hydrophobic interactions with binding pockets -2 to 0 appear to be the main determinant for the orientation and sequence position of peptide binding.

-	~~==Function==~~	+	Structural Studies on the Forward and Reverse Binding Modes of Peptides to the Chaperone DnaK.,Zahn M, Berthold N, Kieslich B, Knappe D, Hoffmann R, Strater N J Mol Biol. 2013 Apr 2. pii: S0022-2836(13)00208-8. doi:, 10.1016/j.jmb.2013.03.041. PMID:23562829<ref>PMID:23562829</ref>
-	~~[[http://www.uniprot.org/uniprot/DNAK_ECOLI DNAK_ECOLI]] Plays an essential role in~~ the ~~initiation~~ of ~~phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein~~ to ~~release lambda O and P proteins from~~ the ~~preprimosomal complex.~~ DnaK ~~is also involved in chromosomal DNA replication~~, ~~possibly through an analogous interaction with the DnaA protein~~. ~~Also participates actively in the response to hyperosmotic shock~~.~~[HAMAP~~-~~Rule:MF_00332] [[http://www.uniprot.org/uniprot/PYRRH_PYRAP PYRRH_PYRAP]] Antibacterial peptide. Affects Gram~~-~~negative bacteria E~~.~~coli 1106~~, P.~~aeruginosa, E~~.~~coli D22 and E~~.~~cloacae and Gram-positive bacteria M~~.~~luteus and B~~.~~subtilis~~.	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4hyb]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4HYB OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:023562829</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Escherichia coli k-12]]		[[Category: Escherichia coli k-12]]
-	[[Category: Straeter, N.]]	+	[[Category: Straeter, N]]
-	[[Category: Zahn, M.]]	+	[[Category: Zahn, M]]
	[[Category: Antimicrobial peptide]]		[[Category: Antimicrobial peptide]]
	[[Category: Chaperone]]		[[Category: Chaperone]]
	[[Category: Peptide binding protein]]		[[Category: Peptide binding protein]]

OCA at 04:33, 18 July 2013

2013-07-18T04:33:22Z

←Older revision		Revision as of 04:33, 18 July 2013
Line 8:		Line 8:
	==About this Structure==		==About this Structure==
	[[4hyb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HYB OCA].		[[4hyb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HYB OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:023562829</ref><references group="xtra"/><references/>
	[[Category: Escherichia coli k-12]]		[[Category: Escherichia coli k-12]]
	[[Category: Straeter, N.]]		[[Category: Straeter, N.]]

OCA at 20:25, 17 April 2013

2013-04-17T20:25:13Z

←Older revision		Revision as of 20:25, 17 April 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4hyb\| PDB=4hyb \| SCENE= }}
		+	===Crystal structure of the substrate binding domain of E.coli DnaK in complex with pyrrhocoricin_LYZI (residues 1 to 10)===
		+	{{ABSTRACT_PUBMED_23562829}}

-	~~The entry 4hyb~~ is ~~ON HOLD~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/DNAK_ECOLI DNAK_ECOLI]] Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.[HAMAP-Rule:MF_00332] [[http://www.uniprot.org/uniprot/PYRRH_PYRAP PYRRH_PYRAP]] Antibacterial peptide. Affects Gram-negative bacteria E.coli 1106, P.aeruginosa, E.coli D22 and E.cloacae and Gram-positive bacteria M.luteus and B.subtilis.

-	~~Authors~~: ~~Zahn, M~~., Straeter, N.	+	==About this Structure==
-		+	[[4hyb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HYB OCA].
-	~~Description~~: ~~Crystal structure of the substrate~~ binding ~~domain of E.coli DnaK in complex with pyrrhocoricin_LYZI~~	+	[[Category: Escherichia coli k-12]]
		+	[[Category: Straeter, N.]]
		+	[[Category: Zahn, M.]]
		+	[[Category: Antimicrobial peptide]]
		+	[[Category: Chaperone]]
		+	[[Category: Peptide binding protein]]

OCA at 10:02, 13 February 2013

2013-02-13T10:02:11Z

←Older revision		Revision as of 10:02, 13 February 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4hyb is ON HOLD ~~until sometime in the future~~	+	The entry 4hyb is ON HOLD

	Authors: Zahn, M., Straeter, N.		Authors: Zahn, M., Straeter, N.

	Description: Crystal structure of the substrate binding domain of E.coli DnaK in complex with pyrrhocoricin_LYZI		Description: Crystal structure of the substrate binding domain of E.coli DnaK in complex with pyrrhocoricin_LYZI

OCA at 11:01, 19 December 2012

2012-12-19T11:01:31Z

←Older revision		Revision as of 11:01, 19 December 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4hyb is ON HOLD	+	The entry 4hyb is ON HOLD until sometime in the future

	Authors: Zahn, M., Straeter, N.		Authors: Zahn, M., Straeter, N.

	Description: Crystal structure of the substrate binding domain of E.coli DnaK in complex with pyrrhocoricin_LYZI		Description: Crystal structure of the substrate binding domain of E.coli DnaK in complex with pyrrhocoricin_LYZI

OCA: Protected "4hyb" [edit=sysop:move=sysop]

2012-11-21T09:09:46Z

Protected "4hyb" [edit=sysop:move=sysop]

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Revision as of 09:09, 21 November 2012